CARACTERIZACIÓN Y EXTRACCIÓN DE LA LISOZIMA DE LA CLARA DE HUEVO

ROMEO OLIVÁN, ANA
ENGIN, EVREN DORUK (dir.)

ANEL BERNAL, ALBERTO (ponente)

Universidad de Zaragoza, CIEN, 2015
Departamento de Bioquímica y Biología Molecular y Celular, Área de Bioquímica y Biología Molecular

Graduado en Biotecnología

Resumen: Lysozyme is a small protein (14kDa) that occurs in almost all body fluids, and tissues of animal organisms. It exhibits bacteriolytic activity due to its ability of breaking bacterial cell walls. The demand of this enzyme has increased because of its diverse uses in pharmacy or food industry. Different methods for isolation have been proposed. Most of them are used in laboratory practice to obtain the pure enzyme of high activity, however only some of these methods are feasible on a commercial scale. The most useful method of lysozyme extraction are chromatography tecnhniques. Other methods, such as crystallization, aqueous two-phase extraction or membrane filtration, have also been reported. In this work, we studied a two-step protocol for the lysozyme extraction from chicken egg white, based on a protein precipitation coupled with chromatography. Three precipitation agents (polyethilenglycol, ammonium sulfate and sodium chloride) and four types of chromatography (cation-exchange chromatography, hydrophobic interaction chromatography, gel filtration chromatography and affinity chromatography) were assayed to determine the efficiency of each methodology. The most efficient methodology was the combination of protein precipitation using 3% polyethilenglycol and ion exchange chromatography, obtaining lysozyme of great purity and the activity was as high as 72 U/ml

Tipo de Trabajo Académico: Trabajo Fin de Grado